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Structural Biology: A Century-long Journey into an Unseen World.

Curry S - Interdiscip Sci Rev (2015)

Bottom Line: Since then the toolbox of structural biology has been augmented by other physical techniques, including nuclear magnetic resonance spectroscopy, electron microscopy, and solution scattering of X-rays and neutrons.Together these have transformed our understanding of the molecular basis of life.Here I review the major and most recent developments in structural biology that have brought us to the threshold of a landscape of astonishing molecular complexity.

View Article: PubMed Central - PubMed

Affiliation: Department of Life Sciences, Imperial College London, UK.

ABSTRACT

When the first atomic structures of salt crystals were determined by the Braggs in 1912-1913, the analytical power of X-ray crystallography was immediately evident. Within a few decades the technique was being applied to the more complex molecules of chemistry and biology and is rightly regarded as the foundation stone of structural biology, a field that emerged in the 1950s when X-ray diffraction analysis revealed the atomic architecture of DNA and protein molecules. Since then the toolbox of structural biology has been augmented by other physical techniques, including nuclear magnetic resonance spectroscopy, electron microscopy, and solution scattering of X-rays and neutrons. Together these have transformed our understanding of the molecular basis of life. Here I review the major and most recent developments in structural biology that have brought us to the threshold of a landscape of astonishing molecular complexity.

No MeSH data available.


Related in: MedlinePlus

Cryo-EM: (a) a cryo-electron micrograph of bacterial ribosomes, (b) class average images derived from averaging the images of ribosome particles determined to have the same orientation, (c) a high-resolution 3D reconstruction of the ribosome.Images are adapted from Bai et al. 2013 under the terms of a Creative Commons 3.0 Attribution Licence
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Figure 0003: Cryo-EM: (a) a cryo-electron micrograph of bacterial ribosomes, (b) class average images derived from averaging the images of ribosome particles determined to have the same orientation, (c) a high-resolution 3D reconstruction of the ribosome.Images are adapted from Bai et al. 2013 under the terms of a Creative Commons 3.0 Attribution Licence

Mentions: The loss of resolving power is due in part to the imperfections of electromagnetic lenses — the best ones are comparable to ‘using a the bottom of a Coca Cola bottle as a magnifying glass’ (Williams and Carter 2009). But it also arises as a result of the damage inflicted on biological samples by the beam, which means that the illuminating doses of electrons have to be kept to a minimum, a constraint that makes for noisy, low-contrast images (Masters 2009). Electron micrographs are grainy and monochrome and, to the untutored eye, somewhat reminiscent of the images beamed back to Earth from planetary probes before the advent of high-resolution digital photography (Figure 3a). There is also another price to pay for the resolution gains of EM: because of the strong interaction of electrons with matter, electron microscopes require high vacuums to prevent scattering of the beam by air molecules, an environment not well suited to the study of living systems. Only samples that are dried or preserved by cryo-cooling can be examined.


Structural Biology: A Century-long Journey into an Unseen World.

Curry S - Interdiscip Sci Rev (2015)

Cryo-EM: (a) a cryo-electron micrograph of bacterial ribosomes, (b) class average images derived from averaging the images of ribosome particles determined to have the same orientation, (c) a high-resolution 3D reconstruction of the ribosome.Images are adapted from Bai et al. 2013 under the terms of a Creative Commons 3.0 Attribution Licence
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4697198&req=5

Figure 0003: Cryo-EM: (a) a cryo-electron micrograph of bacterial ribosomes, (b) class average images derived from averaging the images of ribosome particles determined to have the same orientation, (c) a high-resolution 3D reconstruction of the ribosome.Images are adapted from Bai et al. 2013 under the terms of a Creative Commons 3.0 Attribution Licence
Mentions: The loss of resolving power is due in part to the imperfections of electromagnetic lenses — the best ones are comparable to ‘using a the bottom of a Coca Cola bottle as a magnifying glass’ (Williams and Carter 2009). But it also arises as a result of the damage inflicted on biological samples by the beam, which means that the illuminating doses of electrons have to be kept to a minimum, a constraint that makes for noisy, low-contrast images (Masters 2009). Electron micrographs are grainy and monochrome and, to the untutored eye, somewhat reminiscent of the images beamed back to Earth from planetary probes before the advent of high-resolution digital photography (Figure 3a). There is also another price to pay for the resolution gains of EM: because of the strong interaction of electrons with matter, electron microscopes require high vacuums to prevent scattering of the beam by air molecules, an environment not well suited to the study of living systems. Only samples that are dried or preserved by cryo-cooling can be examined.

Bottom Line: Since then the toolbox of structural biology has been augmented by other physical techniques, including nuclear magnetic resonance spectroscopy, electron microscopy, and solution scattering of X-rays and neutrons.Together these have transformed our understanding of the molecular basis of life.Here I review the major and most recent developments in structural biology that have brought us to the threshold of a landscape of astonishing molecular complexity.

View Article: PubMed Central - PubMed

Affiliation: Department of Life Sciences, Imperial College London, UK.

ABSTRACT

When the first atomic structures of salt crystals were determined by the Braggs in 1912-1913, the analytical power of X-ray crystallography was immediately evident. Within a few decades the technique was being applied to the more complex molecules of chemistry and biology and is rightly regarded as the foundation stone of structural biology, a field that emerged in the 1950s when X-ray diffraction analysis revealed the atomic architecture of DNA and protein molecules. Since then the toolbox of structural biology has been augmented by other physical techniques, including nuclear magnetic resonance spectroscopy, electron microscopy, and solution scattering of X-rays and neutrons. Together these have transformed our understanding of the molecular basis of life. Here I review the major and most recent developments in structural biology that have brought us to the threshold of a landscape of astonishing molecular complexity.

No MeSH data available.


Related in: MedlinePlus